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Title Handbook of flavoproteins. Volume 2, Complex flavoproteins, dehydrogenases and physical methods [electronic resource] / edited by Russ Hille, Susan Miller, Bruce Palfey.
Published Berlin ; Boston : De Gruyter, c2013.
Book Cover

 Electronic Book  QP552.F54 H36 2013 v.2eb    ONLINE
Description 1 online resource : ill. (some col.)
Note Print version cataloged as a monographic set by the Library of Congress.
Bibliography Includes bibliographical references and index.
Contents Preface; 1 The reaction mechanisms of Groups A and B flavoprotein monooxygenases; 1.1 Introduction; 1.2 Enzymes acting upon aromatic substrates -- Group A; 1.2.1 Reactions catalyzed; 1.2.2 Protein structures; 1.2.3 Detailed mechanism of PHBH; Reductive half-reaction; Oxidative half-reaction; Hydroxylation chemistry; Summary; 1.3 Enzymes acting upon non-aromatic substrates -- Group B; 1.3.1 Reactions catalyzed and subclasses; BVMOs; FMOs; NMOs; YUCCAs; 1.3.2 Structural features; 1.4 References
2 Flavin-dependent monooxygenases in siderophore biosynthesis2.1 Iron, an essential but scarce nutrient; 2.2 Siderophores; 2.2.1 Siderophores are important virulence factors; 2.2.2 Structural diversity of siderophores; 2.3 Flavin-dependent N-hydroxylating monooxygenases; 2.4 Catalytic cycle of NMOs; 2.4.1 Flavin reduction in NMOs; 2.4.2 Flavin oxidation in NMOs; 2.5 Three-dimensional structure of NMOs; 2.5.1 FAD-binding domain; 2.5.2 NADPH-binding domain; 2.5.3 L-Ornithine-binding domain; 2.6 The structural basis of substrate specifi city in NMOs
2.7 Mechanism of stabilization of the C4a-hydroperoxyfl avin by NADP+2.8 Activation of NMOs by amino acid binding; 2.9 Unusual NMOs; 2.10 High-throughput screening assay to identify inhibitors of NMOs; 2.11 Conclusions; 2.12 References; 3 The flavin monooxygenases; 3.1 Introduction; 3.2 Occurrence and classifi cation; 3.2.1 Amino acid sequence motifs; 3.2.2 DNA screening; 3.3 Single-component fl avin monooxygenases; 3.3.1 Subclass A; 3.3.2 Subclass B; 3.3.3 Subclass C; 3.3.4 Subclass D; 3.3.5 Subclass E; 3.3.6 Subclass F; 3.4 Conclusions; 3.5 References
4 Structure and catalytic mechanism of NADPH-cytochrome P450 oxidoreductase: a prototype of the difl avin oxidoreductase family of enzymes4.1 Introduction; 4.2 Properties of CYPOR fl avins; 4.3 Domain structure and function; 4.4 Membrane binding domain (MBD); 4.5 FMN domain; 4.6 Cytochrome P450 binding: role of the FMN domain and connecting domain; 4.7 FAD domain; 4.8 Mechanism of hydride transfer; 4.9 Interfl avin electron transfer; 4.10 FMN to heme electron transfer; 4.11 P450 catalysis; 4.12 Other CYPOR electron acceptors; 4.13 CYPOR domain movement and control of electron transfer
4.14 Physiological functions of CYPOR and effects of CYPOR defi ciency4.15 Human CYPOR defi ciency (PORD); 4.16 Contribution of CYPOR to inter-individual variation in human drug metabolism; 4.17 Unanswered questions and future directions; 4.18 References; 5 The xanthine oxidoreductase enzyme family: xanthine dehydrogenase, xanthine oxidase, and aldehyde oxidase; 5.1 Introduction; 5.2 Overall structures; 5.3 Reaction mechanism; 5.4 Electron transfer from the molybdenum center to other redox-active centers; 5.5 Reaction of FAD with NAD+ or molecular oxygen
Note 5.6 Inhibitors of xanthine oxidoreductase
Description based on online resource; title from digital title page (viewed on Oct. 21, 2013).
Subject Flavoproteins.
Related Names Hille, Russ.
Miller, Susan, 1955 December 21-
Palfey, Bruce.
Alternate Title Complex flavoproteins, dehydrogenases and physical methods
Related To Print version: Miller, Susan Handbook of flavoproteins. Berlin ; De Gruyter, c2013. Handbook of Flavoproteins : Volume 2 Complex Flavoproteins, Dehydrogenases and Physical Methods Berlin : De Gruyter,c2013 9783110298284
ISBN 3110298341